Non-electrostatic binding and self-association of amyloid β-peptide on the surface of tightly packed phosphatidylcholine membranes

Mayumi Yoda, Takashi Miura, Hideo Takeuchi

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

Self-association of amyloid β-peptide (Aβ) is considered to be an initial step in the development of Alzheimer's disease and is known to be promoted by negatively charged lipid membranes. We have examined the possibility of non-electrostatic Aβ-membrane interaction by using neutral phosphatidylcholine lipids. Fluorescence and circular dichroism spectra have clearly shown that Aβ binds to the phosphatidylcholine membrane in the lamellar gel phase but not in the ripple gel or liquid crystalline phase, indicating the importance of the tight lipid packing characteristic of the lamellar gel phase. The Aβ-membrane binding occurs at both low and high salt concentrations, ensuring the non-electrostatic nature of the interaction. The membrane-bound Aβ molecule takes a monomeric α-helical or self-associated β-sheet structure depending on the temperature, peptide/lipid ratio, and salt concentration. The flat surface of tightly packed phosphatidylcholine membranes appears to serve as a platform for non-electrostatic binding and self-association of Aβ.

Original languageEnglish
Pages (from-to)56-59
Number of pages4
JournalBiochemical and biophysical research communications
Volume376
Issue number1
DOIs
Publication statusPublished - 2008 Nov 7

Keywords

  • Amyloid β-peptide
  • Circular dichroism
  • Lipid phase transition
  • Peptide secondary structure
  • Peptide-lipid interaction
  • Phosphatidylcholine
  • Self-association

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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